Glial expression of the 90-kDa heat shock protein (HSP90) and the 94-kDa glucose-regulated protein (GRP94) following an excitotoxic lesion in the mouse hippocampus

Glia ◽  
2004 ◽  
Vol 48 (3) ◽  
pp. 250-258 ◽  
Author(s):  
Gye Sun Jeon ◽  
Sang Wook Park ◽  
Dong Woon Kim ◽  
Je Hoon Seo ◽  
Jaeyoung Cho ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Mouse Hippocampus ◽  
Excitotoxic Lesion ◽  
Glucose Regulated Protein

Two stress proteins of the endoplasmic reticulum bind denatured collagen

1990 ◽  
Vol 68 (7-8) ◽  
pp. 1057-1061 ◽  
Author(s):  
Devki Nandan ◽  
Eric H. Ball ◽  
Bishnu D. Sanwal
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Level ◽  
Stress Proteins ◽  
Fold Increase ◽  
Low Ph ◽  
Simple Method ◽  
Collagen Binding ◽  
Glucose Regulated Protein

A differentiation-related gelatin-binding 46 kilodalton (kDa) glycoprotein in myoblasts (GP46, colligin) shares several properties with the 78-kDa glucose-regulated protein (GRP78), including location in the endoplasmic reticulum and related C-terminal sequences. These similarities extend to stress inducibility, since we find that GP46 is a heat-shock protein; its synthesis is elevated at 42 °C, resulting in a two- to three-fold increase in protein level. Further, GRP78 is a gelatin-binding protein; together with GP46 it is retained on gelatin–Sepharose beads. GRP78 and GP46 do not interact; each protein can be individually eluted, GP46 at low pH and GRP78 by ATP. These results suggest that the proteins have distinct roles in the synthesis of collagen and point to a simple method for purification.Key words: stress proteins, collagen-binding proteins, endoplasmic reticulum, 78-kilodalton glucose-regulated protein, 46-kilodalton glycoprotein.

Neuronal induction of 72-kDa heat shock protein following methamphetamine-induced hyperthermia in the mouse hippocampus

1993 ◽  
Vol 626 (1-2) ◽  
pp. 351-356 ◽  
Author(s):  
Satoshi Goto ◽  
Kojiro Korematsu ◽  
Taro Oyama ◽  
Kazumichi Yamada ◽  
Jun-ichiro Hamada ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Induced Hyperthermia ◽  
Mouse Hippocampus

scholarly journals Estrogenic regulation of murine uterine 90-kilodalton heat shock protein gene expression.

1989 ◽  
Vol 9 (8) ◽  
pp. 3567-3570 ◽  
Author(s):  
G Shyamala ◽  
Y Gauthier ◽  
S K Moore ◽  
M G Catelli ◽  
S J Ullrich
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Gene ◽  
Mrna Level ◽  
Target Tissue ◽  
Protein Levels ◽  
Specific Manner ◽  
Estrogenic Regulation ◽  
Glucose Regulated Protein

Murine uterine steady-state protein levels of the 90-kilodalton heat shock protein (HSP90) have been demonstrated recently to be increased by estrogen in a target tissue- and steroid-specific manner (C. Ramachandran, M.G. Catelli, W. Schneider, and G. Shyamala, Endocrinology 123:956-961, 1988). We now report that this regulation occurred with both the HSP86 and HSP84 forms of HSP90 as well as with the 94-kilodalton glucose-regulated protein. At the mRNA level, this response was greatest for HSP86 (15-fold). In contrast, estradiol had no significant effect on HSP70.

Estrogenic regulation of murine uterine 90-kilodalton heat shock protein gene expression

1989 ◽  
Vol 9 (8) ◽  
pp. 3567-3570
Author(s):  
G Shyamala ◽  
Y Gauthier ◽  
S K Moore ◽  
M G Catelli ◽  
S J Ullrich
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Gene ◽  
Mrna Level ◽  
Target Tissue ◽  
Protein Levels ◽  
Specific Manner ◽  
Estrogenic Regulation ◽  
Glucose Regulated Protein

Murine uterine steady-state protein levels of the 90-kilodalton heat shock protein (HSP90) have been demonstrated recently to be increased by estrogen in a target tissue- and steroid-specific manner (C. Ramachandran, M.G. Catelli, W. Schneider, and G. Shyamala, Endocrinology 123:956-961, 1988). We now report that this regulation occurred with both the HSP86 and HSP84 forms of HSP90 as well as with the 94-kilodalton glucose-regulated protein. At the mRNA level, this response was greatest for HSP86 (15-fold). In contrast, estradiol had no significant effect on HSP70.

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